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A recombinant human basic fibroblast growth factor CS23 mutein (rhbFGF-CS23) obtained from Escherichia coli cells has proliferation-stimulating activity for a fetal bovine heart endothelial cell line, ATCC CRL 1395 (biological activity), and strong affinity for heparin (heparin-affinity) similarly to the natural human basic fibroblast growth factor. Plural species having different kinds of heparin-affinity were formed by acetylation of rhbFGF-CS23 with acetic anhydride. To clarify the relationship between the sites with heparin-affinity and the biologically active sites, we have investigated the acetylation sites by peptide mapping and the biological activity of the acetylated species. Consequently, the sites with heparin-affinity in rhbFGF-CS23 are found to be Lys26, Lys119, Lys125, Lys129, and Lys135 in the primary structure, and these sites with heparin-affinity except Lys26 are also clarified to be very important to retain the biological activity of the factor.

Relationship between Biological Activity and Heparin-Affinity Sites of Recombinant Human Basic Fibroblast Growth Factor CS23 Mutein